Biochimica et Biophysica Acta 1988-04-14

Substrate specificity of an acylaminopeptidase that catalyzes the cleavage of the blocked amino termini of peptides.

W M Jones, J M Manning

Index: Biochim. Biophys. Acta 953(3) , 357-60, (1988)

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Abstract

An acylaminopeptidase purified from human red cells cleaves acetylated dipeptides in the decreasing order of acetyl-Ala, acetyl-Met, acetyl-Ser, acetyl-Gly and acetyl-Val. In addition, it was also found that the nature of the second amino-acid residue influenced the rate of cleavage of the blocked N-terminus: charged residues at the second position lead to reduced rates of cleavage. The possible use of this enzyme for structural studies on blocked peptide or protein substrates is evaluated.

Related Compounds

  • N-Acetyl-DL-meth...
  • N-Acetyl-DL-meth...
  • N-acetyl-L-methio...
  • Ac-Gly-OH
  • N-Acetyl-L-alanin...

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